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P16050 (LOX15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arachidonate 15-lipoxygenase

Short name=15-LOX
Short name=15-LOX-1
EC=1.13.11.33
Alternative name(s):
12/15-lipoxygenase
Arachidonate 12-lipoxygenase, leukocyte-type
Short name=12-LOX
EC=1.13.11.31
Arachidonate omega-6 lipoxygenase
Gene names
Name:ALOX15
Synonyms:LOG15
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. Beside its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass. Ref.13

Catalytic activity

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate. Ref.10

Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate. Ref.10

Cofactor

Binds 1 iron ion per subunit By similarity.

Pathway

Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis.

Subunit structure

Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade. Ref.13

Subcellular location

Cytoplasmcytosol. Cell membrane. Lipid droplet. Note: Translocates from the cytosol to the plasma membrane when stimulated by IL13/interleukin-13 and in macrophages binding apoptotic cells. Ref.1 Ref.12 Ref.13

Tissue specificity

Expressed in airway epithelial cells. Ref.13

Induction

Up-regulated by UV-irradiation. Ref.11

Involvement in disease

Disease susceptibility may be associated with variations affecting the gene represented in this entry. Met at position 560 may confer interindividual susceptibility to coronary artery disease (CAD) (Ref.14). Ref.14

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentCell membrane
Cytoplasm
Lipid droplet
Membrane
   Coding sequence diversityPolymorphism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic cell clearance

Inferred from sequence or structural similarity. Source: UniProtKB

arachidonic acid metabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

bone mineralization

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to interleukin-13

Inferred from mutant phenotype Ref.13. Source: UniProtKB

hepoxilin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Traceable author statement PubMed 10200270. Source: ProtInc

leukotriene metabolic process

Traceable author statement. Source: Reactome

lipoxin A4 biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

lipoxygenase pathway

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of adaptive immune response

Inferred from sequence or structural similarity. Source: UniProtKB

ossification

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylethanolamine biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of actin filament polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell-substrate adhesion

Inferred from direct assay PubMed 11278875. Source: UniProtKB

regulation of engulfment of apoptotic cell

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of peroxisome proliferator activated receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

wound healing

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay Ref.13. Source: UniProtKB

lipid particle

Inferred from direct assay Ref.12. Source: UniProtKB

membrane

Inferred from direct assay Ref.13. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionarachidonate 12-lipoxygenase activity

Inferred from direct assay Ref.10. Source: UniProtKB

arachidonate 15-lipoxygenase activity

Inferred from direct assay Ref.10. Source: UniProtKB

eoxin A4 synthase activity

Traceable author statement. Source: Reactome

iron ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9
Chain2 – 662661Arachidonate 15-lipoxygenase
PRO_0000220697

Regions

Domain2 – 114113PLAT
Domain115 – 662548Lipoxygenase

Sites

Metal binding3601Iron; catalytic By similarity
Metal binding3651Iron; catalytic By similarity
Metal binding5401Iron; catalytic By similarity
Metal binding5441Iron; catalytic By similarity
Metal binding6621Iron; via carboxylate; catalytic By similarity

Natural variations

Natural variant901D → H. Ref.4
Corresponds to variant rs11568142 [ dbSNP | Ensembl ].
VAR_018746
Natural variant1021G → V.
Corresponds to variant rs41439950 [ dbSNP | Ensembl ].
VAR_035036
Natural variant1031N → K. Ref.4
Corresponds to variant rs11568099 [ dbSNP | Ensembl ].
VAR_018747
Natural variant2051R → Q. Ref.4
Corresponds to variant rs11568101 [ dbSNP | Ensembl ].
VAR_018748
Natural variant2391V → M.
Corresponds to variant rs3892408 [ dbSNP | Ensembl ].
VAR_035037
Natural variant4611A → P. Ref.6
Corresponds to variant rs17852628 [ dbSNP | Ensembl ].
VAR_035038
Natural variant5601T → M Loss of catalytic activity. Ref.14
Corresponds to variant rs34210653 [ dbSNP | Ensembl ].
VAR_035039

Experimental info

Mutagenesis4181M → V: Catalyzes 15- and 12-lipoxygenation. Ref.10
Sequence conflict461E → V in AAC52118. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P16050 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9ACF7FE7863A045C

FASTA66274,804
        10         20         30         40         50         60 
MGLYRIRVST GASLYAGSNN QVQLWLVGQH GEAALGKRLW PARGKETELK VEVPEYLGPL 

        70         80         90        100        110        120 
LFVKLRKRHL LKDDAWFCNW ISVQGPGAGD EVRFPCYRWV EGNGVLSLPE GTGRTVGEDP 

       130        140        150        160        170        180 
QGLFQKHREE ELEERRKLYR WGNWKDGLIL NMAGAKLYDL PVDERFLEDK RVDFEVSLAK 

       190        200        210        220        230        240 
GLADLAIKDS LNVLTCWKDL DDFNRIFWCG QSKLAERVRD SWKEDALFGY QFLNGANPVV 

       250        260        270        280        290        300 
LRRSAHLPAR LVFPPGMEEL QAQLEKELEG GTLFEADFSL LDGIKANVIL CSQQHLAAPL 

       310        320        330        340        350        360 
VMLKLQPDGK LLPMVIQLQL PRTGSPPPPL FLPTDPPMAW LLAKCWVRSS DFQLHELQSH 

       370        380        390        400        410        420 
LLRGHLMAEV IVVATMRCLP SIHPIFKLII PHLRYTLEIN VRARTGLVSD MGIFDQIMST 

       430        440        450        460        470        480 
GGGGHVQLLK QAGAFLTYSS FCPPDDLADR GLLGVKSSFY AQDALRLWEI IYRYVEGIVS 

       490        500        510        520        530        540 
LHYKTDVAVK DDPELQTWCR EITEIGLQGA QDRGFPVSLQ ARDQVCHFVT MCIFTCTGQH 

       550        560        570        580        590        600 
ASVHLGQLDW YSWVPNAPCT MRLPPPTTKD ATLETVMATL PNFHQASLQM SITWQLGRRQ 

       610        620        630        640        650        660 
PVMVAVGQHE EEYFSGPEPK AVLKKFREEL AALDKEIEIR NAKLDMPYEY LRPSVVENSV 


AI 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and primary structure of human 15-lipoxygenase."
Sigal E., Craik C.S., Highland E., Grunberger D., Costello L.L., Dixon R.A.F., Nadel J.A.
Biochem. Biophys. Res. Commun. 157:457-464(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[2]"Characterization and sequence of an additional 15-lipoxygenase transcript and of the human gene."
Kritzik M.R., Ziober A.F., Dicharry S., Conrad D.J., Sigal E.
Biochim. Biophys. Acta 1352:267-281(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[4]SeattleSNPs variation discovery resource
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-90; LYS-103 AND GLN-205.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-461.
Tissue: Brain and Lung.
[7]"Human 15-lipoxygenase gene promoter: analysis and identification of DNA binding sites for IL-13-induced regulatory factors in monocytes."
Kelavkar U., Wang S., Montero A., Murtagh J., Shah K., Badr K.
Mol. Biol. Rep. 25:173-182(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
[8]"Arachidonate 15-lipoxygenase (omega-6 lipoxygenase) from human leukocytes. Purification and structural homology to other mammalian lipoxygenases."
Sigal E., Grunberger D., Craik C.S., Caughey G.H., Nadel J.A.
J. Biol. Chem. 263:5328-5332(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16.
[9]"Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes."
Izumi T., Raadmark O., Joernvall H., Samuelsson B.
Eur. J. Biochem. 202:1231-1238(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31; 38-45; 157-168 AND 626-631.
Tissue: Eosinophil and Leukocyte.
[10]"A primary determinant for lipoxygenase positional specificity."
Sloane D.L., Leung R., Craik C.S., Sigal E.
Nature 354:149-152(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF MET-418.
[11]"Reciprocal regulation of 12- and 15-lipoxygenases by UV-irradiation in human keratinocytes."
Yoo H., Jeon B., Jeon M.S., Lee H., Kim T.Y.
FEBS Lett. 582:3249-3253(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY UV.
[12]"15(S)-Lipoxygenase-1 associates with neutral lipid droplets in macrophage foam cells: evidence of lipid droplet metabolism."
Weibel G.L., Joshi M.R., Wei C., Bates S.R., Blair I.A., Rothblat G.H.
J. Lipid Res. 50:2371-2376(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells."
Zhao J., O'Donnell V.B., Balzar S., St Croix C.M., Trudeau J.B., Wenzel S.E.
Proc. Natl. Acad. Sci. U.S.A. 108:14246-14251(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN IL13 SIGNALING, INTERACTION WITH PEBP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[14]"A near null variant of 12/15-LOX encoded by a novel SNP in ALOX15 and the risk of coronary artery disease."
Assimes T.L., Knowles J.W., Priest J.R., Basu A., Borchert A., Volcik K.A., Grove M.L., Tabor H.K., Southwick A., Tabibiazar R., Sidney S., Boerwinkle E., Go A.S., Iribarren C., Hlatky M.A., Fortmann S.P., Myers R.M., Kuhn H., Risch N., Quertermous T.
Atherosclerosis 198:136-144(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MET-560, CHARACTERIZATION OF VARIANT MET-560, INVOLVEMENT IN CORONARY ARTERY DISEASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23892 mRNA. Translation: AAA36182.1.
U88317 Genomic DNA. Translation: AAB49305.1.
AK290309 mRNA. Translation: BAF82998.1.
AY505111 Genomic DNA. Translation: AAR84235.1.
AC118754 Genomic DNA. No translation available.
BC029032 mRNA. Translation: AAH29032.1.
U63384 Genomic DNA. Translation: AAC52118.1.
PIRA31349.
RefSeqNP_001131.3. NM_001140.3.
UniGeneHs.73809.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ABTmodel-A2-662[»]
ProteinModelPortalP16050.
SMRP16050. Positions 2-662.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60388N.
STRING9606.ENSP00000293761.

Chemistry

BindingDBP16050.
ChEMBLCHEMBL2903.
DrugBankDB01188. Ciclopirox.
DB00179. Masoprocol.
DB00744. Zileuton.

PTM databases

PhosphoSiteP16050.

Polymorphism databases

DMDM126396.

Proteomic databases

PaxDbP16050.
PRIDEP16050.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000293761; ENSP00000293761; ENSG00000161905.
ENST00000570836; ENSP00000458832; ENSG00000161905.
GeneID246.
KEGGhsa:246.
UCSCuc002fyh.3. human.

Organism-specific databases

CTD246.
GeneCardsGC17M004534.
HGNCHGNC:433. ALOX15.
HPACAB004962.
CAB004963.
HPA013859.
MIM152392. gene.
neXtProtNX_P16050.
PharmGKBPA48.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG133298.
HOVERGENHBG005150.
InParanoidP16050.
KOK00460.
OrthoDBEOG7B05CG.
PhylomeDBP16050.
TreeFamTF105320.

Enzyme and pathway databases

BioCycMetaCyc:HS08621-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00881.

Gene expression databases

ArrayExpressP16050.
BgeeP16050.
CleanExHS_ALOX15.
GenevestigatorP16050.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00305. Lipoxygenase. 2 hits.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiALOX15.
GenomeRNAi246.
NextBio979.
PROP16050.
SOURCESearch...

Entry information

Entry nameLOX15_HUMAN
AccessionPrimary (citable) accession number: P16050
Secondary accession number(s): A8K2P4, Q8N6R7, Q99657
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM